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PDBsum entry 3ilo
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Contents |
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* Residue conservation analysis
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PDB id:
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Transferase
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Title:
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Crystal structure of e. Coli hppk(d97a) in complex with mgampcpp and 6-hydroxymethyl-7,8-dihydropterin
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Structure:
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2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase. Chain: a. Synonym: 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase, hppk, 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, pppk. Engineered: yes. Mutation: yes
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Source:
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Escherichia coli. Organism_taxid: 83333. Strain: k-12. Gene: b0142, foik, folk, jw0138. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.10Å
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R-factor:
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0.143
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R-free:
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0.160
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Authors:
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J.Blaszczyk,Y.Li,H.Yan,X.Ji
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Key ref:
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Y.Li
et al.
Structural and functional roles of residues d95 and d e. Coli hppk.
To be published,
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Date:
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07-Aug-09
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Release date:
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11-Aug-10
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PROCHECK
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Headers
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References
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P26281
(HPPK_ECOLI) -
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase from Escherichia coli (strain K12)
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Seq:
Struc:
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159 a.a.
158 a.a.*
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Key: |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Enzyme class:
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E.C.2.7.6.3
- 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase.
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Pathway:
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Folate Biosynthesis (late stages)
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Reaction:
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6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H+
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6-hydroxymethyl-7,8-dihydropterin
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ATP
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=
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(7,8-dihydropterin-6-yl)methyl diphosphate
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+
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AMP
Bound ligand (Het Group name = )
matches with 68.75% similarity
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+
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H(+)
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Cofactor:
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Mg(2+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Links
